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Study · In vitro (cells) · 2022

3 results

Semax, a Synthetic Regulatory Peptide, Affects Copper-Induced Abeta Aggregation and Amyloid Formation in Artificial Membrane Models.

Sciacca MFM, Naletova I, Giuffrida ML, Attanasio F

ACS chemical neuroscience26 Jan 2022Cited by 10 (Europe PMC)

PMID35080861 (opens in a new tab)PMCIDPMC8855339 (opens in a new tab)DOI10.1021/acschemneuro.1c00707 (opens in a new tab)PepBankPUB-35080861
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Summary

Alzheimer's disease, the most common form of dementia, is characterized by the aggregation of amyloid beta protein (Aβ). The aggregation and toxicity of Aβ are strongly modulated by metal ions and phospholipidic membranes. In particular, Cu2+ ions play a pivotal role in modulating Aβ aggregation. Although in the last decades several natural or synthetic compounds were evaluated as candidate drugs, to date, no treatments are available for the pathology. Multifunctional compounds able to both inhibit fibrillogenesis, and in particular the formation of oligomeric species, and prevent the formation of the Aβ:Cu2+ complex are of particular interest. Here we tested the anti-aggregating properties of a heptapeptide, Semax, an ACTH-like peptide, which is known to form a stable complex with Cu2+ ions and has been proven to have neuroprotective and nootropic effects. We demonstrated through a combination of spectrofluorometric, calorimetric, and MTT assays that Semax not only is able to prevent the formation of Aβ:Cu2+ complexes but also has anti-aggregating and protective properties especially in the presence of Cu2+. The results suggest that Semax inhibits fiber formation by interfering with the fibrillogenesis of Aβ:Cu2+ complexes.
CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study3

3 results from studies that gave the peptide. No result from this study comes from people.

  1. 01LabIn vitro (cells)Activity measurement

    In MTT assays, Semax had protective properties, especially in the presence of Cu2+.

    In plain wordsIn lab tests, Semax showed protective effects, especially with copper present.

    Peptide
    Semax
    Outcome
    IncreaseProtective effect in MTT assays
    Study

    n: not reported in source

    Outcome group
    Neuroprotection · Nervous system and cognition
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Semax not only is able to prevent the formation of Aβ:Cu2+ complexes but also has anti-aggregating and protective properties especially in the presence of Cu2+.
  2. 02LabIn vitro (cell-free)Mechanism

    In cell-free assays, Semax prevented the formation of Abeta:Cu2+ complexes.

    In plain wordsIn lab tests, Semax stopped amyloid beta and copper from forming complexes.

    Peptide
    Semax
    Outcome
    DecreaseFormation of Abeta:Cu2+ complexes
    Study

    n: not reported in source

    Abeta:Cu2+ in artificial membrane models
    Outcome group
    Neuroprotection · Nervous system and cognition
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Semax not only is able to prevent the formation of Aβ:Cu2+ complexes but also has anti-aggregating and protective properties especially in the presence of Cu2+.
  3. 03LabIn vitro (cell-free)Mechanism

    In cell-free assays, Semax had anti-aggregating properties, especially in the presence of Cu2+, and inhibited fiber formation by interfering with fibrillogenesis of Abeta:Cu2+ complexes.

    In plain wordsIn lab tests, Semax reduced clumping and fiber formation of amyloid beta, especially with copper present.

    Peptide
    Semax
    Outcome
    DecreaseAbeta aggregation and fiber formation
    Study

    n: not reported in source

    Abeta:Cu2+ in artificial membrane models
    Outcome group
    Neuroprotection · Nervous system and cognition
    Studied dose
    Dose not stated

    Source sentences

    Summary
    also has anti-aggregating and protective properties especially in the presence of Cu2+.
    1 context sentence
    Summary · context
    The results suggest that Semax inhibits fiber formation by interfering with the fibrillogenesis of Aβ:Cu2+ complexes.

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Version 2Current

    10 Oct 2026, 10:21 UTC

    Study results updated

  2. Version 1

    9 Oct 2026, 03:04 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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